ID   MIC60_AJECN             Reviewed;         666 AA.
AC   A6RBC5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=HCAG_06263;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Component of the MICOS complex, a large protein complex of
CC       the mitochondrial inner membrane that plays crucial roles in the
CC       maintenance of crista junctions, inner membrane architecture, and
CC       formation of contact sites to the outer membrane. Plays a role in
CC       keeping cristae membranes connected to the inner boundary membrane.
CC       Also promotes protein import via the mitochondrial intermembrane space
CC       assembly (MIA) pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC       {ECO:0000305}.
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DR   EMBL; CH476661; EDN10460.1; -; Genomic_DNA.
DR   RefSeq; XP_001538658.1; XM_001538608.1.
DR   AlphaFoldDB; A6RBC5; -.
DR   SMR; A6RBC5; -.
DR   STRING; 339724.A6RBC5; -.
DR   EnsemblFungi; EDN10460; EDN10460; HCAG_06263.
DR   GeneID; 5445102; -.
DR   KEGG; aje:HCAG_06263; -.
DR   VEuPathDB; FungiDB:HCAG_06263; -.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR   PANTHER; PTHR15415; PTHR15415; 1.
DR   Pfam; PF09731; Mitofilin; 2.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..666
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406639"
FT   TOPO_DOM        20..126
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..666
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          25..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          337..482
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        29..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..120
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  73739 MW;  4002978BD85AD703 CRC64;
     MAMYLKSQAV LTLIPQRYHA LARKSNAGRR CSLTPNSATA SQFFQKAASS TSTKPPGPSD
     ADVRSPASPS SRSSLRPESI PKPPQSPPVQ GQTSPGSEVL PPDHESSTPP PPPPPPQGPK
     SSRLRKLLYL FLTAGLAYAG GVWYSLRSDN FYDFFTEYIP YGEEAVLYLE ERDFRNRFPH
     VTKQINRRVT VPKDEGAQVT IPSGSGLSWK VAEEQQEATD MTKKGRRMGT AHANEPTKDI
     KVAEKAKEEV KSKSAAKKED VAANIPIQED LEPQPAKAEE RNLDAPRQPA VPAATTIERL
     VQDKVDEPVV QDLVKVFNDV ISVISADESA SKFAGPIAKA KEELQRIGDR IVALKKDAQE
     SAQEEIRNAH AAFDKSAAEL IRRIDEVRTQ DAAEFREEFE SEREKIARSY QEKVNTELQR
     AHEVAEQRLR NELVEQAIEL NRKFLSDVKT LVENEREGRL SKLAELTANV AELERLTAGW
     SDVVDINLKT QQLQVAVDAV RTTLENSDVP RPFVRELAAV KELASNDEVV AAAIASISPA
     AYQRGIPSAA QLVERFRRVA SEVRKASLLP ENAGITSHAA SLVLSKVMLK KQGLPTGDDV
     ESILTRTENF LEEGNFDEAA REMNSLQGWA KLLSKDWLAD VRQVLEVKQA LEIIETEARL
     RCLQVE